7xsu

Cardiac sodium channel in complex with LqhIII

Method: ELECTRON MICROSCOPY Dmax: 130.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Sodium channel protein type 5 subunit alpha,G protein/GFP fusion protein

Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP

UniProt B7UCZ6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 512–750 Not recorded Alpha-like toxin Lqh3 × 1 (P56678) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 BMA beta-D-mannopyranose × 1 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 6 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B7UCZ6_9RHAB
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1590–1828; UniProt 512–750

Sodium channel protein type 5 subunit alpha,G protein/GFP fusion protein

Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP

UniProt P15389

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–461 Chain A; UniProt 659–1068 Chain A; UniProt 1190–1898 Not recorded Alpha-like toxin Lqh3 × 1 (P56678) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 BMA beta-D-mannopyranose × 1 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 6 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCN5A_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–461; UniProt 1–461 Author chain A; PDBConstruct 462–871; UniProt 659–1068 Author chain A; PDBConstruct 872–1580; UniProt 1190–1898

Alpha-like toxin Lqh3

OrganismNot specified

UniProt P56678

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–67 Not recorded Sodium channel protein type 5 subunit alpha,G protein/GFP fusion protein × 1 (P15389,B7UCZ6) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 BMA beta-D-mannopyranose × 1 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 6 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCL3_LEIHE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–67; UniProt 1–67

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7xsu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xsu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7xsu
Deposition date deposition_date2022-05-15
Structure title titleCardiac sodium channel in complex with LqhIII
Keywords keywordscardiac sodium channel, MEMBRANE PROTEIN, MEMBRANE PROTEIN-TOXIN complex; MEMBRANE PROTEIN/TOXIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier36.28
Radius of gyration Rg (electron density) rg_electron35.21
Forward intensity I(0) i0211424000.00
Molecular weight molecular_weight127320.0 kDa
Excluded volume excluded_volume163530 ų
Envelope volume envelope_volume222660 ų
Hydration-shell volume shell_volume52613 ų
Envelope diameter envelope_diameter140.6
Shell Rg shell_rg41.48
Envelope Rg envelope_rg35.79
Shape Rg shape_rg35.21
Total Rg total_rg35.67
Total atoms total_atoms8969
Residues n_residues1152
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax130.7
Rg (real space) rg_real36.19
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.1140e+08
I(0) uncertainty (real space) i0_real_error3.1690e+06
Rg (reciprocal space) rg_reciprocal36.25
I(0) (reciprocal space) i0_reciprocal211400000.0000
Solution quality estimate total_estimate0.8487
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.5
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.135
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha23980000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.681; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)